Abstract
Differences in the structure of PYY and two important analogs, PYY [3-36] and [Pro34]PYY, are evaluated. Y-receptor subtype ligand binding data are used in conjunction with structural data to develop a model for receptor subtype selective agonists. For PYY it is proposed that potent binding to Y1, Y4 and Y5 receptors requires the juxtaposition of the two termini while Y2 binding only requires the C-terminal helix. Further experiments that delineate between primary and tertiary structure contributions for receptor binding and activation are required to support the hypothesis that tertiary structure is stable enough to influence the expression of PYY's bioactivity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amides / chemistry
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Amino Acid Sequence
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Animals
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DNA, Complementary / metabolism
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Gene Library
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Humans
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Inhibitory Concentration 50
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Ligands
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Models, Molecular
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Molecular Sequence Data
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Peptide YY / chemistry*
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Peptide YY / metabolism
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Peptides / chemistry
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Receptors, Gastrointestinal Hormone / chemistry
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Receptors, Gastrointestinal Hormone / metabolism
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Receptors, Neuropeptide Y / chemistry
Substances
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Amides
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DNA, Complementary
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Ligands
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Peptides
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Receptors, Gastrointestinal Hormone
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Receptors, Neuropeptide Y
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neuropeptide Y-Y1 receptor
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neuropeptide Y2 receptor
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neuropeptide Y5 receptor
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peptide YY receptor
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Peptide YY
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neuropeptide Y4 receptor